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1.
J Sci Food Agric ; 104(4): 2130-2141, 2024 Mar 15.
Article in English | MEDLINE | ID: mdl-37922378

ABSTRACT

BACKGROUND: The consumption of oranges generates huge amounts of pomaces, which are the potential raw materials to increase the nutritional value of the products. RESULTS: In this study, the bioactive composition and flavor volatiles in Lactobacillus fermented orange juice with added pomaces were researched. Results showed that the orange juices blended with pomaces were favorable substrates for Lactobacillus growth and the colony counts reached above 9.0 log CFU mL-1 , total phenolics, total flavonoids, and the antioxidant activity in orange juices were increased significantly after adding pomaces. Some amino acids, such as threonine (P < 0.0001), isoleucine (P < 0.01), and glycine (P < 0.01) were markedly higher in fermented orange juices with pomaces. The flavonoid diversity was more abundant by adding pomace fermentation and most flavonoids showed higher levels in fermented juices with the pomace, Lactobacillus fermentum 252 may transform some flavonoids through deglycosylation and reduction reaction. Furthermore, orange pomace mainly improved the flavor volatiles by increasing terpenoids and alcohol, such as d-limonene and benzyl alcohol, and decreasing volatile acids. CONCLUSION: This study presented a novelty in elevating the nutritional value of juice by the utilization of pomaces, its findings can provide a new way to mine the bioactive ingredient from Citrus by Lactobacillus, and can be used as a guide for the development of new Citrus processing technologies and functional foods. © 2023 Society of Chemical Industry.


Subject(s)
Citrus sinensis , Lactobacillus , Citrus sinensis/chemistry , Antioxidants/analysis , Fruit and Vegetable Juices , Flavonoids/analysis
2.
Ultrason Sonochem ; 101: 106643, 2023 Dec.
Article in English | MEDLINE | ID: mdl-37922721

ABSTRACT

New natural multifunctional polysaccharide and its innovatory extraction technology may be urgently needed for food industries. Our aims were to establish new extraction method and investigate the primary structures, bioactivities and rheological properties of novel E. yadongensis polysaccharide (EYP). Ultrasound assisted mechanical wall-breaking extraction (MAUE) was successfully established for the EYP extraction from a new E. yadongensis. Based on the MAUE with RSM, the polysaccharide yield of 17.92 ± 0.56 % with the optimal parameters of five extraction factors were obtained, and current MAUE was characterized by its high yield, low extraction temperature and short ultrasound time. After the isolation and purification, the EYP as a protein-bound polysaccharide was obtained. FT-IR and NMR analysis showed that the main backbone of the EYP comprised of (1 â†’ 4)-ß-D-glucopyranosyl and (1 â†’ 6)-ɑ-D-mannopyranosyl groups; EYP exhibited significant antioxidant, antibacterial, antitumor, antidiabetic activities, and good viscoelastic properties in low pH solutions (P < 0.05). The EYP may be used as a natural functional and cohesive agent in food industries.


Subject(s)
Chemical Fractionation , Polysaccharides , Spectroscopy, Fourier Transform Infrared , Chemical Fractionation/methods , Polysaccharides/chemistry , Antioxidants/chemistry , Rheology
3.
Food Res Int ; 137: 109457, 2020 11.
Article in English | MEDLINE | ID: mdl-33233133

ABSTRACT

Inhibition of endogenous protease is a rapid and feasible approach to control the proteolysis proceeding of post mortem fish flesh. In the present study, the in vitro inhibitory effects of common edible di- and tri-carboxylic acids and salts on endogenous proteolytic activities as well as myofibrillar disassembly and degradation mediated by crude enzyme of grass carp muscle were investigated. The results showed that among the compounds tested, maleic acid, fumaric acid, tartaric acid and malic acid were the most effective inhibitor for cathepsin B, L and calpain, with IC50 ranging from 7.76 to 30.13 mM, from 32.38 to 65.12 mM, from 1.06 to 6.76 mM, respectively. Also, relatively lower Ki (ranging from 1.04 to 43.21 mM) of these compounds were found towards cathepsin B, L and calpain. Incubation of myofibrillar protein with crude enzyme in the presence of di- and tri-carboxylic compounds could remarkably suppress the dissociation and degradation of myosin heavy chain (MHC), and ameliorate the loss of heat shock protein (HSP) in myofibrils, with tartaric acid and fumaric acid proved more effective than other compounds, possibly implicating their application as potential and efficient inhibitors for quality control of fish muscle products.


Subject(s)
Carps , Myofibrils , Animals , Calpain , Fish Proteins , Peptide Hydrolases
4.
Biomed Res Int ; 2017: 6847532, 2017.
Article in English | MEDLINE | ID: mdl-28638833

ABSTRACT

As an indicator of the antioxidant capability of plants, catalase can detoxify reactive oxygen species (ROS) generated by environmental stresses. Sweet potato is one of the top six most important crops in the world. However, its catalases remain largely unknown. In this study, a catalase encoding gene, IbCAT2 (accession number: KY615708), was identified and cloned from sweet potato cv. Xushu 18. It contained a 1479 nucleotides' open reading frame (ORF). S-R-L, Q-K-L, and a putative calmodulin binding domain were located at the C-terminus of IbCAT2, which suggests that IbCAT2 could be a peroxisomal catalase. Next-generation sequencing (NGS) based quantitative analyses showed that IbCAT2 was mainly expressed in young leaves and expanding tuberous roots under normal conditions. When exposed to 10% PEG6000 or 200 mmol/L NaCl solutions, IbCAT2 was upregulated rapidly in the first 11 days and then downregulated, although different tissues showed different degree of change. Overexpression of IbCAT2 conferred salt and drought tolerance in Escherichia coli and Saccharomyces cerevisiae. The positive response of IbCAT2 to abiotic stresses suggested that IbCAT2 might play an important role in stress responses.


Subject(s)
Catalase , Ipomoea batatas , Plant Proteins , Stress, Physiological , Catalase/chemistry , Catalase/genetics , Catalase/isolation & purification , Catalase/metabolism , Gene Expression Regulation, Enzymologic/physiology , Gene Expression Regulation, Plant/physiology , Ipomoea batatas/enzymology , Ipomoea batatas/genetics , Open Reading Frames , Plant Leaves/enzymology , Plant Leaves/genetics , Plant Proteins/genetics , Plant Proteins/isolation & purification , Plant Proteins/metabolism , Plant Tubers/enzymology , Plant Tubers/genetics , Recombinant Proteins/genetics , Recombinant Proteins/isolation & purification , Recombinant Proteins/metabolism , Sequence Analysis, DNA
5.
J Food Sci ; 79(10): M2040-7, 2014 Oct.
Article in English | MEDLINE | ID: mdl-25227959

ABSTRACT

The objective of this study was to evaluate the relative effects and interactions of combined soaking treatment using citric acid (CTA) and apple polyphenol (APP) at mild heating temperatures for the inactivation of the external and internal microflora (mesophilic aerobic bacteria, mesophilic anaerobic bacteria, and fungi) in Chinese Tuber indicum, as well as to analyze the microbiological and sensory changes under modified atmosphere packaging (MAP)- and vacuum atmosphere packaging (VAC)-packed Chinese T. indicum stored at 4 °C for up to 55 d. Chinese T. indicum was soaked with CTA and APP alone or in combination for 10, 20, and 30 min at 35, 45, and 55 °C. A disinfection method using CTA and APP (3% CTA + 3% APP for 20 min at 45 °C) was obtained. Under this set of combination, the experimental values of microbial counts of mesophilic aerobic bacteria, mesophilic anaerobic bacteria, and fungi were 2.31 ± 0.4 log CFU/g, <1.0 log CFU/g, and <1.0 log CFU/g, respectively. Through the analysis of sensory qualities and microbial populations for MAP- or VAC-packed Chinese T. indicum, the shelf life of soaked truffles was prolonged to 45 or 40 d, respectively. The synergistic effect of CTA and APP may provide valuable insight into the reduction of microorganisms on fresh truffles.


Subject(s)
Ascomycota , Food Microbiology , Food Packaging/methods , Food Storage , Atmosphere , Bacteria/classification , Bacteria/isolation & purification , Food Additives , Temperature , Vacuum
6.
Can J Microbiol ; 59(4): 245-51, 2013 Apr.
Article in English | MEDLINE | ID: mdl-23586748

ABSTRACT

Phytases play a very important role in increasing phytate digestion and reducing phosphorus pollution in the environment, and phytate-degrading bacteria have a ubiquitous distribution in the environment. Due to its extremely harsh environment, the Tibetan Plateau breeds possibly abundant, extreme microorganisms. In this research, 67 phytate-degrading bacteria were isolated from different habitats in the Tibetan Plateau. Among all isolates, 40.3% were screened from farmland, 25.3% from wetland, 4.5% from saline-alkaline soil, 7.5% from hot springs, and 22.4% from lawns, which showed that the distribution of the phytate-degrading bacteria varied with habitats. By the PCR-RFLP method, 16 different species were identified and named, 4 of which are reported for the first time as phytate-degrading bacteria, that is, Uncultured Enterococcus sp. GYPB01, Bacillaceae bacterium strain GYPB05, Endophytic bacterium strain GYPB16, and Shigella dysenteria strain GYPB22. Through the assay of phytase activity of 16 strains, Klebsiella sp. strain GYPB15 displayed the highest capability of phytase production. Through analysis of the optimum pH, the optimum temperature, and the thermal stability of enzyme from 16 strains, some especial phytate-degrading bacteria were obtained. Our findings clearly indicate a good relation between the composition of the soils from the different environments in the Tibetan Plateau and populations of cultivable phytate-degrading bacteria. Moreover, extreme harsh soils are logically the best soils in which to find some strains of phytate-degrading bacteria for exploiting in the fields of biotechnology and industry.


Subject(s)
Bacteria/classification , Bacteria/isolation & purification , Phytic Acid/metabolism , Soil Microbiology , 6-Phytase/genetics , Bacteria/enzymology , Bacteria/genetics , Ecosystem , Klebsiella/genetics , Phylogeny , Polymerase Chain Reaction , Polymorphism, Restriction Fragment Length
7.
J Biosci Bioeng ; 116(1): 34-8, 2013 Jul.
Article in English | MEDLINE | ID: mdl-23453854

ABSTRACT

The major objective of this study was to engineer lactic acid bacteria to produce the enzyme phytase from a gene native to Bacillus subtilis GYPB04. The phytase gene (phyC) of B. subtilis GYPB04 was cloned into the plasmid pMG36e for expression in Lactococcus lactis. The enzyme activity in L. lactis cultured in GM17 broth was 20.25 U/mL at 36°C. The expressed phytase was characterized as active in a pH range of 2.0-9.0 at a temperature range of 20-80°C, with an optimum pH of 5.5-6.5 and temperature of 60°C. When cultured in food-grade milk broth, the transformed L. lactis grew to an OD(600 nm) value of 1.05 and had a phytase yield of 13.58 U/mL. In same broth under optimized conditions for cell growth and phytase production, the transformant reached an OD(600 nm) value of 1.68 and a phytase yield of 42.12 U/mL, representing approximately 1.6-fold and 3.1-fold increases, respectively, compared to growth in natural milk broth. Fermentation was scaled to 5 L under optimized conditions, and product analysis revealed a final OD(600 nm) value of 1.89 and an extracellular enzyme activity of 24.23 U/mL. The results of this study may be used in the dairy fermentation industry for the development of functional, healthy yogurts and other fermented dairy foods that provide both active phytase and viable probiotics to the consumer.


Subject(s)
6-Phytase/genetics , Lactococcus lactis/genetics , Milk/microbiology , 6-Phytase/biosynthesis , 6-Phytase/metabolism , Animals , Bacillus subtilis/enzymology , Bacillus subtilis/genetics , Fermentation , Lactococcus lactis/growth & development , Lactococcus lactis/metabolism , Plasmids/genetics , Probiotics , Temperature
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